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| Expression, Purification and Characterization of β-N-acetylglucosaminidase from Aeromonas veronii B565 |
| LIU Yang1, YANG Ya-lin2, ZHANG Yu-ting2, RAN Chao2, ZHOU Zhi-gang1,2 |
1. Fisheries Colloge of Huazhong Agricultural University, Wuhan 430070, China;
2. Feed Research Institute of Chinese Academy of Agriculture Sciences, Beijing 100081, China |
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Abstract β-N-acetylglucosaminidase (chitobiase) gene nag565 from Aeromonas veronii B565 was cloned and expressed in E.coli. The deduced amino acid sequence of nag565 is most similar to those of other Aeromonas sp. The deduced sequence of NAG565 contained one putative signal peptide, one carbohydrate binding domain, two catalytic domain of glycosyl hydrolase family 20, and one chitobiase/beta-hexosaminidase C-terminal domain. Purified mature NAG565 has a specific activity of 7328 U/mg. NAG565 had an optimal activity at pH 7.0 and 37℃, showed good resistance to various metal ions and digestion by proteases. NAG565 retained almost all its optimal activity under aquaculture conditions (20~30℃ and pH 7.0). Taken together, the A. veronii B565 NAG565 may adapt to the environment of cultured fish gastrointestinal tract and may be potential aquacultural feed additive, facilitating the effective utilization of chitin.
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Received: 23 October 2014
Published: 25 February 2015
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